2026-07-21T08:44:13Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/169422024-09-27T23:21:25Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609

00925njm 22002777a 4500 dc Ballegeer, Marlies author van Scherpenzeel, Revina C author Delgado-Romero, Teresa author Iglesias-Caballero, Maria author Garcia-Barreno, Blanca author Pandey, Shubham author Rush, Scott A author Kolkman, Joost A author Mas-Lloret, Vicente author McLellan, Jason S author Saelens, Xavier author 2024 Human metapneumovirus (hMPV) is an important respiratory pathogen for which no licensed antivirals or vaccines exist. Single-domain antibodies represent promising antiviral biologics that can be easily produced and formatted. We describe the isolation and detailed characterization of two hMPV-neutralizing single-domain antibodies that are directed against the fusion protein F. One of these single-domain antibodies broadly neutralizes hMPV A and B strains, can prevent proteolytic maturation of F, and binds to an epitope in the F trimer interface. This suggests that hMPV pre-F undergoes trimer opening or "breathing" on infectious virions, exposing a vulnerable site for neutralizing antibodies. Finally, we show that this single-domain antibody, fused to a human IgG1 Fc, can protect cotton rats against hMPV replication, an important finding for potential future clinical applications. mBio. 2024 Jan 16;15(1):e0212223. 10.1128/mbio.02122-23 2150-7511 mBio 38117059 http://hdl.handle.net/20.500.12105/16942 Fusion protein Human metapneumovirus Single-domain antibody Structure A neutralizing single-domain antibody that targets the trimer interface of the human metapneumovirus fusion protein